Michael Whippo
IUUR STEM Summer Research Program
Major: Chemistry
Mentors: Charles Dann III, Morgan Nyman, Martha Oakley, and Melissa Blunck
Designing anticancer treatments that target specific receptors could lead to less toxic and more effective therapeutics. Folate receptor beta (FRβ) is known to be overexpressed in tumor-associated macrophages (TAMs) and can serve as a target for therapeutics [1]. m909 is a monoclonal antibody with an affinity for FRβ and could be mutated in order to allow for tighter binding to FRβ [2]. Through the use of site-directed mutagenesis (SDM), it could be possible to increase the binding affinity of the mutated antibody for FRβ and, in turn, develop a useful receptor-specific anticancer therapeutic. To improve the binding affinity of the m909 antibody for FRβ, SDM was used to make specific and deliberate mutations to the DNA sequence that codes for the protein antibody. Our group investigated six possible mutated forms of the m909 antibody through the use of the SDM PCR technique. We have not yet been able to successfully perform the second PCR for this project. The next steps in this research project are to carry out the second PCR so that the plasmid mutants can be sequenced. Then the plasmid mutants can be grown up in HB2151E cells prior to expression, purification, and finally, folate receptor assays.
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